Nan Li,Ruiyan Wang,Zeyuan Deng,Jianqun Zhou,Wenwen Li,Qian Du,Liufeng Zheng
Sucrose emerges as a metal-ion chelating agent with excellent stability that may increase metal-ion absorption. This study aimed to characterize the structure of zinc–sucrose complex and investigate its ability to promote zinc absorption in Caco-2 monolayer cells and mice. Based on the results of the inductively coupled plasma emission spectrometer (ICP-ES), scanning electron microscopy–energy-dispersive X-ray spectroscopy (SEM-EDX), and Fourier transform infrared spectroscopy (FT-IR), it can be inferred that zinc and sucrose were chelated at a 1:1 ratio, with the hydroxyl groups playing a significant role. The Caco-2 monolayer cell model revealed that zinc–sucrose complex increased the amount of zinc uptake, retention, and transport in a dose- and time-dependent manner. Through the upregulation of genes and proteins for ZIP4, MT1, and DMT1, treatment with zinc–sucrose complex improved the proportion of absorbed zinc utilized for transport compared to ZnCl2 (26.21 ± 4.96 versus 8.50 ± 1.51%). Pharmacokinetic analysis of mice confirmed the zinc absorption-promoting effect of zinc–sucrose complex, as indicated by the considerably higher serum zinc level (4.16 ± 0.53 versus 2.56 ± 0.45 mg/L) and intestinal ZIP4, MT1, and DMT1 gene expression than ZnCl2. Further treatment of different zinc channel inhibitors and CETSA demonstrated the direct interaction of zinc–sucrose complex with ZIP4 protein and ZIP4-mediated cellular transport of zinc–sucrose complex. These findings provide a novel insight into the zinc absorption-promoting mechanism of zinc–sucrose complex, which could be used as an ingredient in functional foods to treat zinc deficiency.
Zinc is an essential mineral for human health, and its deficiency can lead to various health issues. Oysters ( Crassostrea gigas ) are known to be a rich source of protein-bound zinc. Oyster peptides were complexed with zinc sulfate (ZnSO 4 ) to be oyster peptide-zinc chelates (OPZs) that offer potential as a valuable zinc supplement. The complexation of zinc with oyster peptides induces conformational changes in the peptides, altering their overall spatial arrangement. This could potentially impact their functions and properties. OPZs have demonstrated enhanced physical and gastrointestinal stability, as they are resistant to digestion by pepsin and trypsin. The research has shown that OPZs can modulate the expression of key proteins involved in zinc binding (MT1), peptide transport (PePT1), and zinc transport (ZIP4 and ZnT1) in enterocytes. By regulating the proteins expression, OPZs have the potential to affect zinc absorption and homeostasis. Furthermore, OPZs have been found to enhance zinc absorption through dual pathways compared to the single pathway of inorganic zinc. Additionally, they have the potential to improve zinc bioaccessibility and bioavailability, meaning they can make zinc more easily absorbed by the body and readily available for use.
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